Secreted Nucleobindin-2 Inhibits 3T3-L1 Adipocyte Differentiation
| Autor: | Yuko Tagaya, Shuichi Okada, Koshi Hashimoto, Tetsurou Satoh, Aya Osaki, Hiroyuki Shimizu, Masatomo Mori, Atsuko Miura, Kihachi Ohshima, Masanobu Yamada |
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| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
insulin
medicine.medical_treatment Nerve Tissue Proteins Biology Biochemistry DNA-binding protein Article chemistry.chemical_compound Mice Structural Biology Adipocyte Calcium-binding protein 3T3-L1 Cells medicine Adipocytes Cyclic AMP Animals Humans Nucleobindins 3T3-L1 chemistry.chemical_classification Adipogenesis Insulin Binding protein Calcium-Binding Proteins General Medicine Nucleobindin-2 Cell biology Nucleobindin 2 Amino acid Rats DNA-Binding Proteins chemistry Nesfatin-1 GST |
| Zdroj: | Protein and Peptide Letters |
| ISSN: | 1875-5305 0929-8665 |
| Popis: | Nucleobindin-2 is a 420 amino acid EF-hand Ca²⁺ binding protein that can be further processed to generate an 82 amino terminal peptide termed Nesfatin-1. To examine the function of secreted Nucleobindin-2 in adipocyte differentiation, cultured 3T3-L1 cells were incubated with either 0 or 100 nM of GST, GST-Nucleobindin-2, prior to and during the initiation of adipocyte differentiation. Nucleobindin-2 treatment decreased neutral lipid accumulation (Oil-Red O staining) and expression of several marker genes for adipocyte differentiation (PPARγ, aP2, and adipsin). When Nucleobindin- 2 was constitutively secreted into cultured medium, cAMP content and insulin stimulated CREB phosphorylation were significantly reduced. On the other hand, intracellularly overexpressed Nucleobindin-2 failed to affect cAMP content and CREB phosphorylation. Taken together, these data indicate that secreted Nucleobindin-2 is a suppressor of adipocyte differentiation through inhibition of cAMP production and insulin signal. |
| Databáze: | OpenAIRE |
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